메뉴 건너뛰기




Volumn 587, Issue 17, 2013, Pages 2860-2867

A new regulatory principle for in vivo biochemistry: Pleiotropic low affinity regulation by the adenine nucleotides - Illustrated for the glycolytic enzymes of Saccharomyces cerevisiae

Author keywords

ATP; Biology; Energetics; Enzyme kinetics; Systems; Yeast glycolysis model

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ALCOHOL; ALCOHOL DEHYDROGENASE; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE 6 PHOSPHATE ISOMERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEXOKINASE; PHOSPHOGLYCERATE KINASE; PHOSPHOGLYCERATE MUTASE; PYRUVATE DECARBOXYLASE; PYRUVATE KINASE; TRIOSEPHOSPHATE ISOMERASE;

EID: 84883052726     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.07.013     Document Type: Article
Times cited : (15)

References (30)
  • 3
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: A brief overview
    • H. Kitano Systems biology: a brief overview Science 295 2002 1662 1664
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 6
    • 33746927955 scopus 로고    scopus 로고
    • International alliances for quantitative modeling in systems biology
    • H. Kitano International alliances for quantitative modeling in systems biology Mol. Syst. Biol. 1 2005 2005 0007
    • (2005) Mol. Syst. Biol. , vol.1 , Issue.2005 , pp. 0007
    • Kitano, H.1
  • 9
    • 33645116839 scopus 로고    scopus 로고
    • Yeast systems biology to unravel the network of life
    • R. Mustacchi, S. Hohmann, and J. Nielsen Yeast systems biology to unravel the network of life Yeast 23 2006 227 238
    • (2006) Yeast , vol.23 , pp. 227-238
    • Mustacchi, R.1    Hohmann, S.2    Nielsen, J.3
  • 11
    • 0037020260 scopus 로고    scopus 로고
    • Reproducibility of oligonucleotide microarray transcriptome analyses. An interlaboratory comparison using chemostat cultures of Saccharomyces cerevisiae
    • M.D. Piper, P. Daran-Lapujade, C. Bro, B. Regenberg, S. Knudsen, J. Nielsen, and J.T. Pronk Reproducibility of oligonucleotide microarray transcriptome analyses. An interlaboratory comparison using chemostat cultures of Saccharomyces cerevisiae J. Biol. Chem. 277 2002 37001 37008
    • (2002) J. Biol. Chem. , vol.277 , pp. 37001-37008
    • Piper, M.D.1    Daran-Lapujade, P.2    Bro, C.3    Regenberg, B.4    Knudsen, S.5    Nielsen, J.6    Pronk, J.T.7
  • 13
    • 0026710123 scopus 로고
    • Effect of benzoic acid on metabolic fluxes in yeasts: A continuous-culture study on the regulation of respiration and alcoholic fermentation
    • C. Verduyn, E. Postma, W.A. Scheffers, and J.P. Van Dijken Effect of benzoic acid on metabolic fluxes in yeasts: a continuous-culture study on the regulation of respiration and alcoholic fermentation Yeast 8 1992 501 517
    • (1992) Yeast , vol.8 , pp. 501-517
    • Verduyn, C.1    Postma, E.2    Scheffers, W.A.3    Van Dijken, J.P.4
  • 15
    • 0012926979 scopus 로고    scopus 로고
    • Effect of specific growth rate on fermentative capacity of baker's yeast
    • P. Van Hoek, J.P. Van Dijken, and J.T. Pronk Effect of specific growth rate on fermentative capacity of baker's yeast Appl. Environ. Microbiol. 64 1998 4226 4233
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4226-4233
    • Van Hoek, P.1    Van Dijken, J.P.2    Pronk, J.T.3
  • 16
    • 71549133050 scopus 로고    scopus 로고
    • Enzyme kinetics and computational modeling for systems biology
    • M.L. Johnson, L Brand, Academic Press San Diego (Chapter 22)
    • P. Mendes, H. Messiha, N. Malys, and S. Hoops Enzyme kinetics and computational modeling for systems biology M.L. Johnson, L Brand, Methods in Enzymology 2009 Academic Press San Diego 583 599 (Chapter 22)
    • (2009) Methods in Enzymology , pp. 583-599
    • Mendes, P.1    Messiha, H.2    Malys, N.3    Hoops, S.4
  • 19
    • 84861131751 scopus 로고    scopus 로고
    • Testing biochemistry revisited: How in vivo metabolism can be understood from in vitro enzyme kinetics
    • K. Van Eunen, J.A. Kiewiet, H.V. Westerhoff, and B.M. Bakker Testing biochemistry revisited: how in vivo metabolism can be understood from in vitro enzyme kinetics PLoS Comput. Biol. 8 2012 e1002483
    • (2012) PLoS Comput. Biol. , vol.8 , pp. 1002483
    • Van Eunen, K.1    Kiewiet, J.A.2    Westerhoff, H.V.3    Bakker, B.M.4
  • 20
    • 0026715777 scopus 로고
    • A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH
    • W. De Koning, and K. Van Dam A method for the determination of changes of glycolytic metabolites in yeast on a subsecond time scale using extraction at neutral pH Anal. Biochem. 204 1992 118 123
    • (1992) Anal. Biochem. , vol.204 , pp. 118-123
    • De Koning, W.1    Van Dam, K.2
  • 21
    • 0030722640 scopus 로고    scopus 로고
    • Glycolytic flux is conditionally correlated with ATP concentration in Saccharomyces cerevisiae: A chemostat study under carbon- or nitrogen-limiting conditions
    • C. Larsson, A. Nilsson, A. Blomberg, and L. Gustafsson Glycolytic flux is conditionally correlated with ATP concentration in Saccharomyces cerevisiae: a chemostat study under carbon- or nitrogen-limiting conditions J. Bacteriol. 179 1997 7243 7250
    • (1997) J. Bacteriol. , vol.179 , pp. 7243-7250
    • Larsson, C.1    Nilsson, A.2    Blomberg, A.3    Gustafsson, L.4
  • 22
    • 78549252106 scopus 로고    scopus 로고
    • Time-resolved measurements of intracellular ATP in the yeast Saccharomyces cerevisiae using a new type of nanobiosensor
    • V.C. Ozalp, T.R. Pedersen, L.J. Nielsen, and L.F. Olsen Time-resolved measurements of intracellular ATP in the yeast Saccharomyces cerevisiae using a new type of nanobiosensor J. Biol. Chem. 285 2010 37579 37588
    • (2010) J. Biol. Chem. , vol.285 , pp. 37579-37588
    • Ozalp, V.C.1    Pedersen, T.R.2    Nielsen, L.J.3    Olsen, L.F.4
  • 24
    • 0020490497 scopus 로고
    • Quantification of the contribution of various steps to the control of mitochondrial respiration
    • A.K. Groen, R.J. Wanders, H.V. Westerhoff, R. van der Meer, and J.M. Tager Quantification of the contribution of various steps to the control of mitochondrial respiration J. Biol. Chem. 257 1982 2754 2757
    • (1982) J. Biol. Chem. , vol.257 , pp. 2754-2757
    • Groen, A.K.1    Wanders, R.J.2    Westerhoff, H.V.3    Van Der Meer, R.4    Tager, J.M.5
  • 26
    • 0038819563 scopus 로고    scopus 로고
    • Multiplex inhibitor screening and kinetic constant determinations for yeast hexokinase using mass spectrometry based assays
    • H. Gao, and J.A. Leary Multiplex inhibitor screening and kinetic constant determinations for yeast hexokinase using mass spectrometry based assays J. Am. Soc. Mass Spectrom. 14 2003 173 181
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 173-181
    • Gao, H.1    Leary, J.A.2
  • 27
    • 0035969954 scopus 로고    scopus 로고
    • Regulation of phosphotransferase activity of hexokinase 2 from Saccharomyces cerevisiae by modification at serine-14
    • R. Golbik, M. Naumann, A. Otto, E. Muller, J. Behlke, R. Reuter, G. Hubner, and T.M. Kriegel Regulation of phosphotransferase activity of hexokinase 2 from Saccharomyces cerevisiae by modification at serine-14 Biochemistry 40 2001 1083 1090
    • (2001) Biochemistry , vol.40 , pp. 1083-1090
    • Golbik, R.1    Naumann, M.2    Otto, A.3    Muller, E.4    Behlke, J.5    Reuter, R.6    Hubner, G.7    Kriegel, T.M.8
  • 28
    • 0033842957 scopus 로고    scopus 로고
    • Analysis of aluminum-yeast hexokinase interaction: Modifications on protein structure and functionality
    • J.M. Socorro, R. Olmo, C. Teijon, M.D. Blanco, and J.M. Teijon Analysis of aluminum-yeast hexokinase interaction: modifications on protein structure and functionality J. Protein Chem. 19 2000 199 208
    • (2000) J. Protein Chem. , vol.19 , pp. 199-208
    • Socorro, J.M.1    Olmo, R.2    Teijon, C.3    Blanco, M.D.4    Teijon, J.M.5
  • 29
    • 0020484780 scopus 로고
    • Substrate synergism and the kinetic mechanism of yeast hexokinase
    • R.E. Viola, F.M. Raushel, A.R. Rendina, and W.W. Cleland Substrate synergism and the kinetic mechanism of yeast hexokinase Biochemistry 21 1982 1295 1302
    • (1982) Biochemistry , vol.21 , pp. 1295-1302
    • Viola, R.E.1    Raushel, F.M.2    Rendina, A.R.3    Cleland, W.W.4
  • 30
    • 0000870544 scopus 로고
    • Die Kinetik der Invertinwirkung
    • L. Michaelis, and M.L. Menten Die Kinetik der Invertinwirkung Biochem. Z. 49 1913 333 369
    • (1913) Biochem. Z. , vol.49 , pp. 333-369
    • Michaelis, L.1    Menten, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.